SitesBLAST
Comparing WP_012991206.1 NCBI__GCF_000025605.1:WP_012991206.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
1bxrA Structure of carbamoyl phosphate synthetase complexed with the atp analog amppnp (see paper)
54% identity, 96% coverage: 2:512/532 of query aligns to 560:1054/1073 of 1bxrA
- active site: K634 (= K76), R715 (= R157), G721 (= G163), G722 (= G164), S745 (= S187), E761 (= E203), D769 (= D211), Q829 (= Q271), E841 (= E283), N843 (= N285), R848 (= R290), P901 (= P359)
- binding phosphoaminophosphonic acid-adenylate ester: R675 (= R117), V713 (≠ L155), R715 (= R157), L720 (= L162), G721 (= G163), G722 (= G164), M725 (= M167), D753 (= D195), F755 (≠ Y197), L756 (= L198), E761 (= E203), A785 (= A227), G786 (= G228), V787 (= V229), H788 (= H230), Q829 (= Q271), E841 (= E283), N843 (= N285), R848 (= R290)
- binding manganese (ii) ion: Q829 (= Q271), E841 (= E283), E841 (= E283), N843 (= N285)
- binding L-ornithine: E783 (= E225), D791 (= D233), E892 (= E350), L907 (= L365), D1041 (≠ T499), T1042 (= T500)
Sites not aligning to the query:
- active site: 129, 169, 174, 176, 202, 215, 243, 283, 285, 299, 301, 303, 307, 338, 507
- binding phosphoaminophosphonic acid-adenylate ester: 129, 167, 169, 174, 175, 176, 210, 211, 215, 240, 241, 243, 244, 285, 299, 306, 376
- binding manganese (ii) ion: 299, 301
P00968 Carbamoyl phosphate synthase large chain; Carbamoyl phosphate synthetase ammonia chain; EC 6.3.4.16; EC 6.3.5.5 from Escherichia coli (strain K12) (see 6 papers)
54% identity, 96% coverage: 2:512/532 of query aligns to 560:1054/1073 of P00968
- R715 (= R157) binding
- H754 (≠ A196) binding
- L756 (= L198) binding
- E761 (= E203) binding
- G786 (= G228) binding
- V787 (= V229) binding
- H788 (= H230) binding
- S789 (= S231) binding
- Q829 (= Q271) binding ; binding
- E841 (= E283) binding ; binding ; binding
- N843 (= N285) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 129 binding
- 169 binding
- 175 binding
- 176 binding
- 208 binding
- 210 binding
- 215 binding
- 241 binding
- 242 binding
- 243 binding
- 285 binding ; binding
- 299 binding ; binding ; binding
- 301 binding
Q42601 Carbamoyl phosphate synthase arginine-specific large chain, chloroplastic; CPS; CPSase; Ammonium-dependent carbamoyl phosphate synthetase; Arginine-specific carbamoyl phosphate synthetase, ammonia chain; Glutamine-dependent carbamoyl phosphate synthetase; Protein VENOSA 3; EC 6.3.4.16; EC 6.3.5.5 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
51% identity, 100% coverage: 2:531/532 of query aligns to 650:1177/1187 of Q42601
- A844 (= A183) mutation to T: In ven3-4; reduced plant size and reticulate leaf phenotype.
- P1014 (= P367) mutation to L: In ven3-1; reticulate leaf phenotype.
Sites not aligning to the query:
- 149 P→L: In ven3-2; reduced plant size and reticulate leaf phenotype.
- 587 G→E: In ven3-3; reticulate leaf phenotype.
1t36A Crystal structure of e. Coli carbamoyl phosphate synthetase small subunit mutant c248d complexed with uridine 5'-monophosphate (see paper)
52% identity, 96% coverage: 2:512/532 of query aligns to 560:1039/1058 of 1t36A
- active site: K634 (= K76), R715 (= R157), E746 (= E203), D754 (= D211), Q814 (= Q271), E826 (= E283), N828 (= N285), R833 (= R290), P886 (= P359)
- binding adenosine-5'-diphosphate: R715 (= R157), M718 (= M167), F740 (≠ Y197), L741 (= L198), E746 (= E203), A770 (= A227), G771 (= G228), V772 (= V229), H773 (= H230), E826 (= E283), P894 (= P367)
- binding manganese (ii) ion: Q814 (= Q271), E826 (= E283)
- binding L-ornithine: E768 (= E225), D776 (= D233), E877 (= E350), L892 (= L365), D1026 (≠ T499), T1027 (= T500)
- binding uridine-5'-monophosphate: K939 (= K412), T959 (= T432), G961 (= G434), T962 (= T435), K978 (= K451), N1000 (= N473), T1001 (= T474), T1002 (≠ P475), S1011 (≠ A484), I1014 (= I487)
Sites not aligning to the query:
- active site: 129, 169, 174, 176, 202, 215, 243, 283, 285, 299, 301, 303, 307, 338, 507
- binding adenosine-5'-diphosphate: 129, 167, 169, 174, 175, 176, 208, 210, 211, 215, 240, 241, 242, 243, 285, 298, 299, 376
- binding manganese (ii) ion: 285, 299, 299, 301
- binding phosphate ion: 174, 175, 243, 299, 301, 303, 306
1c3oA Crystal structure of the carbamoyl phosphate synthetase: small subunit mutant c269s with bound glutamine (see paper)
52% identity, 96% coverage: 2:512/532 of query aligns to 560:1039/1058 of 1c3oA
- active site: K634 (= K76), R715 (= R157), E746 (= E203), D754 (= D211), Q814 (= Q271), E826 (= E283), N828 (= N285), R833 (= R290), P886 (= P359)
- binding adenosine-5'-diphosphate: R715 (= R157), M718 (= M167), F740 (≠ Y197), L741 (= L198), E746 (= E203), A770 (= A227), G771 (= G228), V772 (= V229), H773 (= H230), S774 (= S231), E826 (= E283)
- binding manganese (ii) ion: Q814 (= Q271), E826 (= E283)
- binding L-ornithine: E768 (= E225), D776 (= D233), E877 (= E350), L892 (= L365), D1026 (≠ T499), T1027 (= T500)
Sites not aligning to the query:
- active site: 129, 169, 174, 176, 202, 215, 243, 283, 285, 299, 301, 303, 307, 338, 507
- binding adenosine-5'-diphosphate: 129, 167, 169, 174, 176, 210, 211, 215, 240, 241, 243, 244, 285, 298, 299, 376
- binding glutamine: 528, 537, 538, 554
- binding manganese (ii) ion: 285, 299, 299, 301
- binding phosphate ion: 174, 175, 243, 299, 301, 303, 306
1ce8A Carbamoyl phosphate synthetase from escherichis coli with complexed with the allosteric ligand imp (see paper)
52% identity, 96% coverage: 2:512/532 of query aligns to 560:1039/1058 of 1ce8A
- active site: K634 (= K76), R715 (= R157), E746 (= E203), D754 (= D211), Q814 (= Q271), E826 (= E283), N828 (= N285), R833 (= R290), P886 (= P359)
- binding adenosine-5'-diphosphate: R715 (= R157), F740 (≠ Y197), L741 (= L198), E746 (= E203), A770 (= A227), G771 (= G228), V772 (= V229), H773 (= H230), S774 (= S231), E826 (= E283)
- binding inosinic acid: S933 (= S406), K939 (= K412), T959 (= T432), G961 (= G434), T962 (= T435), K978 (= K451), V979 (= V452), I986 (≠ V459), N1000 (= N473), T1001 (= T474), T1002 (≠ P475), D1010 (= D483), S1011 (≠ A484), V1013 (≠ Y486)
- binding manganese (ii) ion: Q814 (= Q271), E826 (= E283)
- binding L-ornithine: E768 (= E225), D776 (= D233), E877 (= E350), L892 (= L365), Y1025 (= Y498), D1026 (≠ T499), T1027 (= T500)
Sites not aligning to the query:
- active site: 129, 169, 174, 176, 202, 215, 243, 283, 285, 299, 301, 303, 307, 338, 507
- binding adenosine-5'-diphosphate: 129, 167, 169, 174, 176, 210, 211, 215, 240, 241, 242, 243, 285, 298, 299, 376
- binding manganese (ii) ion: 174, 285, 299, 299, 301
- binding L-ornithine: 528, 537, 538, 552, 554
- binding phosphate ion: 174, 175, 243, 299, 301, 303, 306
1a9xA Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis (see paper)
52% identity, 96% coverage: 2:512/532 of query aligns to 560:1039/1058 of 1a9xA
- active site: K634 (= K76), D754 (= D211), P886 (= P359)
- binding adenosine-5'-diphosphate: R715 (= R157), M718 (= M167), F740 (≠ Y197), L741 (= L198), E746 (= E203), A770 (= A227), G771 (= G228), V772 (= V229), H773 (= H230), E826 (= E283)
- binding manganese (ii) ion: Q814 (= Q271), E826 (= E283)
- binding L-ornithine: E768 (= E225), D776 (= D233), E877 (= E350), L892 (= L365), Y1025 (= Y498), D1026 (≠ T499), T1027 (= T500)
Sites not aligning to the query:
- active site: 202, 338, 507
- binding adenosine-5'-diphosphate: 129, 167, 169, 174, 175, 176, 210, 215, 240, 241, 242, 243, 244, 285, 298, 299, 376
- binding manganese (ii) ion: 285, 299, 299, 301
- binding phosphate ion: 175, 243, 299, 301, 303, 306
Q09794 Multifunctional protein ura1; Pyrimidine-specific carbamoyl phosphate synthase-aspartate carbamoyl transferase; CPSase-ATCase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
39% identity, 100% coverage: 2:531/532 of query aligns to 1014:1534/2244 of Q09794
- S1119 (≠ P107) modified: Phosphoserine
Sites not aligning to the query:
- 1881 modified: Phosphoserine
- 1885 modified: Phosphoserine
P07259 Multifunctional protein URA2; Pyrimidine-specific carbamoyl phosphate synthase-aspartate carbamoyl transferase; CPSase-ATCase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (see paper)
39% identity, 96% coverage: 4:512/532 of query aligns to 982:1485/2214 of P07259
Sites not aligning to the query:
- 1857 modified: Phosphoserine; by PKA
P07756 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Rattus norvegicus (Rat) (see 2 papers)
36% identity, 96% coverage: 4:513/532 of query aligns to 976:1478/1500 of P07756
- S1331 (= S371) modified: carbohydrate, O-linked (GlcNAc) serine
- T1332 (= T372) modified: carbohydrate, O-linked (GlcNAc) threonine
- T1391 (= T432) mutation to V: 400-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
- T1394 (= T435) mutation to A: 900-fold increase in the activation constant of NAG. 3-fold decrease in the reaction rate at saturation of NAG.
- W1410 (≠ K451) mutation to K: 60-fold increase in the activation constant of NAG.
- N1437 (= N473) mutation to D: 70-fold increase in the activation constant of NAG.
- N1440 (≠ T476) mutation to D: 110-fold increase in the activation constant of NAG. Modifies the specificity for the activator: Binds Phe-NAG considerably better than NAG.
Sites not aligning to the query:
- 537 modified: carbohydrate, O-linked (GlcNAc) serine; alternate
Q8C196 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Mus musculus (Mouse) (see 2 papers)
36% identity, 96% coverage: 4:513/532 of query aligns to 976:1478/1500 of Q8C196
- K1291 (≠ E322) modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
Sites not aligning to the query:
- 44 modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
- 287 modified: N6-acetyllysine; alternate; modified: N6-succinyllysine; alternate
P31327 Carbamoyl-phosphate synthase [ammonia], mitochondrial; Carbamoyl-phosphate synthetase I; CPSase I; EC 6.3.4.16 from Homo sapiens (Human) (see 22 papers)
36% identity, 96% coverage: 4:513/532 of query aligns to 976:1478/1500 of P31327
- I986 (= I14) to T: in CPS1D; associated with V-304; dbSNP:rs1553516442
- G987 (= G15) to C: in CPS1D; may affect splicing; dbSNP:rs1553516443
- K1074 (≠ T102) modified: N6-glutaryllysine; alternate
- K1150 (≠ T178) modified: N6-glutaryllysine
- K1168 (≠ A196) modified: N6-glutaryllysine; alternate
- K1183 (≠ D211) modified: N6-glutaryllysine; alternate
- I1215 (≠ L243) to V: in CPS1D; uncertain significance; dbSNP:rs141373204
- K1224 (= K252) modified: N6-glutaryllysine
- I1254 (≠ L282) to F: in CPS1D; uncertain significance
- F1266 (= F294) to S: in dbSNP:rs1047886
- M1283 (≠ S311) to L: in dbSNP:rs1047887
- K1356 (≠ R396) modified: N6-glutaryllysine; alternate
- K1360 (≠ E400) modified: N6-glutaryllysine; alternate
- LIGI 1363:1366 (≠ FVSV 404:407) natural variant: Missing (in CPS1D; uncertain significance)
- G1376 (≠ D417) to S: no functional consequences; no negative effect on protein stability, enzyme activity and thermal stability; dbSNP:rs140578009
- A1378 (≠ V419) to T: in CPS1D; significant reduction in thermal stability; dbSNP:rs1245373037
- L1381 (≠ F422) to S: in CPS1D; significant loss of protein stability
- T1406 (≠ K447) to N: probable risk factor for PHN; dbSNP:rs1047891
- P1411 (≠ V452) to L: in CPS1D; modestly decreases enzyme activity; dbSNP:rs1202306773
- T1443 (vs. gap) to A: in CPS1D; almost complete loss of enzyme activity; approximately 10-fold decrease in the apparent Vmax for bicarbonate, ammonia and ATP; decreased affinity for NAG
- R1453 (= R488) to Q: in CPS1D; the enzyme is inactive; to W: in CPS1D; the enzyme is inactive; dbSNP:rs933813349
Sites not aligning to the query:
- 55 modified: N6-glutaryllysine; alternate
- 123 S → F: in CPS1D; modestly decreases enzyme activity; S → Y: in CPS1D; uncertain significance
- 171 modified: N6-glutaryllysine; alternate
- 174 R → W: in CPS1D; uncertain significance; dbSNP:rs1553509661
- 176 modified: N6-glutaryllysine
- 207 modified: N6-glutaryllysine; alternate
- 210 modified: N6-glutaryllysine; alternate
- 214 modified: N6-glutaryllysine; alternate
- 219 modified: N6-glutaryllysine; alternate
- 228 modified: N6-glutaryllysine; alternate
- 237 modified: N6-glutaryllysine
- 280 modified: N6-glutaryllysine; alternate
- 304 A → V: in CPS1D; associated with T-986; dbSNP:rs775920437
- 307 modified: N6-glutaryllysine; alternate
- 310 modified: N6-glutaryllysine; alternate
- 337 H → R: in CPS1D; modestly decreases enzyme activity; dbSNP:rs28940283
- 344 T → A: no negative effect on protein stability, enzyme activity and thermal stability; dbSNP:rs1047883
- 355 N → D: in CPS1D; around 80% decrease in enzyme activity; significant reduction in thermal stability; approximately 4-fold decrease in the apparent Vmax for ATP, bicarbonate and ammonia; dbSNP:rs1472190012
- 389 Y → C: in CPS1D; around 40% decrease in enzyme activity; significant loss of thermal stability
- 390 L → R: in CPS1D; significant loss of protein stability
- 401 G → R: in CPS1D; uncertain significance; associated with N-937 in a patient; dbSNP:rs760895692
- 402 modified: N6-glutaryllysine; alternate
- 412 modified: N6-glutaryllysine; alternate
- 438 A → P: in CPS1D; almost complete loss of enzyme activity; dbSNP:rs772497399
- 453 modified: N6-glutaryllysine; alternate
- 458 modified: N6-glutaryllysine; alternate
- 527 modified: N6-glutaryllysine; alternate
- 530 G → V: found in a patient with VACTERL syndrome and postsurgical PHN; uncertain significance; dbSNP:rs1250316045
- 532 modified: N6-glutaryllysine; alternate
- 544 T → M: in CPS1D; almost complete loss of enzyme activity; approximately 60-fold increase in the apparent Km for bicarbonate and approximately 4-fold respective decrease and increase in the apparent Vmax and Km for ammonia; dbSNP:rs121912592
- 553 modified: N6-glutaryllysine; alternate
- 678 Q → P: in CPS1D; results in a poor enzyme expression and solubility; hampers correct enzyme folding
- 728 modified: N6-glutaryllysine
- 757 modified: N6-glutaryllysine; alternate
- 772 modified: N6-glutaryllysine; alternate
- 774 P → L: in CPS1D; the enzyme is inactive
- 793 modified: N6-glutaryllysine; alternate
- 811 modified: N6-glutaryllysine; alternate
- 841 modified: N6-glutaryllysine; alternate
- 843 L → S: in CPS1D; associated in cis with E-875; causes 70% decrease of enzyme activity; significant decrease in protein yield
- 850 R → C: in CPS1D; moderate decrease in protein yield and partial loss of enzyme activity; dbSNP:rs1015051007; R → H: in CPS1D; partial loss of enzyme activity; dbSNP:rs767694281
- 856 modified: N6-glutaryllysine; alternate
- 869 modified: N6-glutaryllysine
- 871 T → P: in CPS1D; significant decrease in protein yield and enzyme activity
- 875 modified: N6-glutaryllysine; alternate; K → E: associated in cis with S-843 in a patient with carbamoyl-phosphate synthase deficiency; does not affect enzyme activity; significant decrease in protein yield and thermal stability; dbSNP:rs147062907
- 889 modified: N6-glutaryllysine; alternate
- 892 modified: N6-glutaryllysine; alternate
- 905 modified: N6-glutaryllysine
- 908 modified: N6-glutaryllysine; alternate
- 911 G → E: in CPS1D; significant decrease in protein yield and enzyme activity; dbSNP:rs1388955593; G → V: in CPS1D; significant decrease in protein yield and enzyme activity
- 913 S → L: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity; dbSNP:rs754706559
- 914 D → G: in CPS1D; significant decrease in protein yield and enzyme activity; D → H: in CPS1D; significant decrease in protein yield and enzyme activity; dbSNP:rs765484849
- 915 modified: N6-glutaryllysine; alternate
- 918 S → P: in CPS1D; significant decrease in protein yield and enzyme activity
- 919 modified: N6-glutaryllysine; alternate
- 932 R → T: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity
- 937 I → N: in CPS1D; associated with R-401; significant decrease in protein yield and enzyme activity; dbSNP:rs760714614
- 949 A → T: in CPS1D; partial loss of enzyme activity and significant decrease in thermal stability; dbSNP:rs537170841
- 958 L → P: in CPS1D; significant decrease in protein yield and enzyme activity
- 959 Y → C: in CPS1D; significant decrease in protein yield and thermal stability; partial loss of enzyme activity; dbSNP:rs1191587211
- 962 Y → C: in CPS1D; significant decrease in protein yield and partial loss of enzyme activity; dbSNP:rs955666400
- 964 G → D: in CPS1D; significant decrease in protein yield and enzyme activity; dbSNP:rs534815243
- 1479 modified: N6-glutaryllysine; alternate
- 1486 modified: N6-glutaryllysine; alternate
- 1491 Y → H: in CPS1D; triggers a large decrease in the apparent affinity for N-acetyl-L-glutamate (NAG); dbSNP:rs1553519513
Q18990 Multifunctional protein pyr-1; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Caenorhabditis elegans (see 3 papers)
36% identity, 99% coverage: 4:529/532 of query aligns to 937:1466/2198 of Q18990
Sites not aligning to the query:
- 1602 H→Q: In cu8; probable loss of dihydroorotase activity. Severe late stage embryonic lethality in 50% of animals. The few surviving mutants have a shorter and thicker pharyngeal isthmus, an abnormal knobbed tail, mild egg-laying defects, moderate fluid accumulation in the coelom and a slower growth. Actin and intermediate filaments are disorganized in the pharynx. Moderate reduction in heparan sulfate levels and increased levels of chondroitin sulfate. In an umps-1 zu456 mutant background, prevents the formation of abnormally enlarged gut granules in embryos. Complete embryonic lethality in a rnst-2 qx245 mutant background.
P05990 Multifunctional protein r; Protein rudimentary; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Drosophila melanogaster (Fruit fly) (see 2 papers)
36% identity, 99% coverage: 3:531/532 of query aligns to 948:1471/2224 of P05990
- E1167 (= E222) mutation to K: Severely diminishes UTP inhibition of CPSase; in Su(b).
Sites not aligning to the query:
- 1883 modified: Phosphoserine
- 1885 modified: Phosphoserine
- 1892 modified: Phosphoserine
- 1894 modified: Phosphoserine
6w2jA Cps1 bound to allosteric inhibitor h3b-374 (see paper)
34% identity, 96% coverage: 4:513/532 of query aligns to 923:1408/1422 of 6w2jA
Sites not aligning to the query:
- active site: 651, 665, 667, 673, 869
- binding (2-fluoranyl-4-methoxy-phenyl)-[(3~{R},5~{R})-4-(2-fluoranyl-4-methoxy-phenyl)carbonyl-3,5-dimethyl-piperazin-1-yl]methanone: 605, 607, 615, 725, 726, 727, 730, 732, 756, 760, 763, 764, 795, 797, 798
- binding zinc ion: 273, 293, 295, 320
6w2jB Cps1 bound to allosteric inhibitor h3b-374 (see paper)
34% identity, 96% coverage: 4:513/532 of query aligns to 865:1350/1364 of 6w2jB
Sites not aligning to the query:
- active site: 593, 607, 609, 615, 811
- binding (2-fluoranyl-4-methoxy-phenyl)-[(3~{R},5~{R})-4-(2-fluoranyl-4-methoxy-phenyl)carbonyl-3,5-dimethyl-piperazin-1-yl]methanone: 547, 549, 557, 668, 669, 672, 673, 698, 702, 705, 706, 737, 739, 740
- binding zinc ion: 273, 293, 295, 320
P20054 Multifunctional protein pyr1-3; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Dictyostelium discoideum (Social amoeba)
35% identity, 97% coverage: 2:516/532 of query aligns to 947:1453/2225 of P20054
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
5douD Crystal structure of human carbamoyl phosphate synthetase i (cps1), ligand-bound form (see paper)
34% identity, 96% coverage: 4:513/532 of query aligns to 934:1419/1430 of 5douD
- active site: A1006 (≠ K76), R1087 (= R157), E1116 (= E203), K1124 (≠ D211), Q1184 (= Q271), E1196 (= E283), N1198 (= N285), R1203 (= R290), R1260 (≠ P359)
- binding adenosine-5'-diphosphate: L1085 (= L155), F1110 (≠ Y197), V1111 (≠ L198), E1116 (= E203), A1140 (= A227), V1142 (= V229), H1143 (= H230), S1144 (= S231), Q1184 (= Q271), L1186 (≠ A273), I1195 (≠ L282), E1196 (= E283)
- binding n-acetyl-l-glutamate: I1307 (≠ V407), Q1308 (≠ A408), T1332 (= T432), A1334 (≠ G434), T1335 (= T435), W1351 (≠ K451), L1379 (≠ T474), T1384 (vs. gap), K1385 (≠ R479), F1386 (≠ A480), N1390 (≠ A484)
Sites not aligning to the query:
- active site: 252, 335, 337, 505, 545, 576, 589, 617, 656, 658, 672, 674, 676, 680, 880
- binding adenosine-5'-diphosphate: 505, 543, 545, 550, 551, 552, 581, 583, 584, 585, 589, 614, 615, 616, 617, 658, 671, 672
- binding magnesium ion: 658, 672, 672, 674
- binding phosphate ion: 550, 551, 617, 672, 674, 676, 679
P08955 Multifunctional protein CAD; Carbamoyl phosphate synthetase 2-aspartate transcarbamylase-dihydroorotase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Mesocricetus auratus (Golden hamster) (see paper)
35% identity, 96% coverage: 3:512/532 of query aligns to 934:1440/2225 of P08955
- S1406 (≠ R481) modified: Phosphoserine; by PKA; mutation to A: No effect on enzyme kinetics.; mutation to D: Increases CPSase activity and reduces sensitivity to feedback inhibition by UTP.
P27708 Multifunctional protein CAD; Carbamoyl phosphate synthetase 2-aspartate transcarbamylase-dihydroorotase; EC 6.3.5.5; EC 3.5.1.2; EC 6.3.4.16; EC 2.1.3.2; EC 3.5.2.3 from Homo sapiens (Human) (see 7 papers)
35% identity, 96% coverage: 3:512/532 of query aligns to 934:1440/2225 of P27708
- S1406 (≠ R481) modified: Phosphoserine; by PKA
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 2 modified: N-acetylalanine
- 33 M → R: in DEE50; uncertain significance; dbSNP:rs751610198
- 177 R → Q: in a colorectal cancer sample; somatic mutation; dbSNP:rs374122292
- 456 modified: Phosphothreonine; by MAPK1
- 735 Y → C: in a colorectal cancer sample; somatic mutation
- 1471 binding ; binding ; H→A: No zinc-binding and no catalytic activity.; H→N: Abolishes dihydroorotase activity.
- 1473 binding ; H→A: No zinc-binding and no catalytic activity.
- 1475 binding
- 1505 binding
- 1512 D→N: No change in catalytic activity.
- 1556 binding via carbamate group; binding via carbamate group; modified: N6-carboxylysine
- 1562 T→A: Abolishes dihydroorotase activity.
- 1563 F→A: Abolishes dihydroorotase activity.
- 1590 binding ; H→A: Abolishes dihydroorotase activity.; H→N: No catalytic activity.
- 1613 binding ; C→S: Reduces dihydroorotase activity.
- 1614 binding ; H→A: Abolishes dihydroorotase activity.
- 1637 binding ; E→T: Abolishes dihydroorotase activity.
- 1642 H→N: 11.5% of wild-type catalytic activity.
- 1661 binding
- 1686 binding ; D→N: Abolishes dihydroorotase activity.
- 1690 binding ; H→N: 3% of wild-type catalytic activity.
- 1702 binding
- 1789:2225 natural variant: Missing (in DEE50; uncertain significance)
- 1859 modified: Phosphoserine; by RPS6KB1 and PKA
- 1873 modified: Phosphoserine; by PKC; in vitro; S→A: Abolishes PMA-induced Thr-456 phosphorylation.
- 1900 modified: Phosphoserine
Query Sequence
>WP_012991206.1 NCBI__GCF_000025605.1:WP_012991206.1
MKKVVILGSGPNRIGQGIEFDYACVQAIFSLREEGVQTIMINCNPETVSTDYDTADRLYF
EPVVLENVLEVIRREKPDGVLIQFGGQTPLKLSLPLRDAGVTILGTPPESIDIAEDRELF
RRLIQKLGLRQPPSEAVRSKEEAIRVAEAIGYPVLVRPSYVLGGRAMRIIYDREELVTYL
EEAVEVSYQRPILIDAYLSDSVEVDVDAIGDGEDFLVGAVMEHIEEAGVHSGDSAASIPP
YTLPSDVVEEIKRQSKEIARSLGVVGLINLQFAVKDGEVYVLEVNPRASRTVPFVSKAIG
YPLAKLAAKVSIGRKLRELVPEVFRRLEEGNVHPCSDFLPSDWNLYCVKEVVFPWNRFPE
VDPVLGPEMKSTGEVMGIDTVFGLAFYKAQLAVGNRLPTEGSVFVSVADKDKPKAVDLVK
GFLELGFEVLATSGTYQYMKEKGLEVKHVLKVSEGRPHVVDMIKNGQISLVINTPTGKRA
RTDAYYIRRAVVQYSVPYTTTVRGGYAMLEAIRCYKNSGGKLTVRALQDIFP
Or try a new SitesBLAST search
SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory